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RLHA_ECOLI
ID   RLHA_ECOLI              Reviewed;         653 AA.
AC   P76104; P76865; P76867; P76868;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=23S rRNA 5-hydroxycytidine C2501 synthase {ECO:0000305};
DE   AltName: Full=Large subunit ribosomal RNA hydroxylation A {ECO:0000303|PubMed:29069499};
GN   Name=rlhA {ECO:0000303|PubMed:29069499}; Synonyms=ydcP;
GN   OrderedLocusNames=b1435, JW1431;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, ACTIVITY REGULATION, SUBUNIT, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF GLU-161; HIS-165; CYS-169; GLN-175; CYS-176; CYS-580 AND
RP   CYS-611.
RX   PubMed=29069499; DOI=10.1093/nar/gkx969;
RA   Kimura S., Sakai Y., Ishiguro K., Suzuki T.;
RT   "Biogenesis and iron-dependency of ribosomal RNA hydroxylation.";
RL   Nucleic Acids Res. 45:12974-12986(2017).
CC   -!- FUNCTION: Responsible for the formation of the 5-hydroxycytidine
CC       modification at the C2501 position (ho5C2501) of 23S rRNA. May be a Fe-
CC       S protein that catalyzes ho5C2501 formation using prephenate as a
CC       hydroxyl group donor. {ECO:0000269|PubMed:29069499}.
CC   -!- ACTIVITY REGULATION: Iron-sulfur clusters and prephenate are required
CC       for ho5C2501 formation. {ECO:0000269|PubMed:29069499}.
CC   -!- SUBUNIT: Interacts with precursors of the 50S ribosomal subunit.
CC       {ECO:0000269|PubMed:29069499}.
CC   -!- INTERACTION:
CC       P76104; P05824: recN; NbExp=3; IntAct=EBI-556974, EBI-548098;
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene results in complete loss of
CC       the ho5C2501 modification. {ECO:0000269|PubMed:29069499}.
CC   -!- SIMILARITY: Belongs to the peptidase U32 family. {ECO:0000305}.
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DR   EMBL; U00096; AAC74517.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15068.1; -; Genomic_DNA.
DR   RefSeq; NP_415952.2; NC_000913.3.
DR   RefSeq; WP_001303492.1; NZ_SSZK01000021.1.
DR   AlphaFoldDB; P76104; -.
DR   SMR; P76104; -.
DR   BioGRID; 4263353; 39.
DR   BioGRID; 850355; 1.
DR   DIP; DIP-11650N; -.
DR   IntAct; P76104; 50.
DR   STRING; 511145.b1435; -.
DR   MEROPS; U32.003; -.
DR   jPOST; P76104; -.
DR   PaxDb; P76104; -.
DR   PRIDE; P76104; -.
DR   EnsemblBacteria; AAC74517; AAC74517; b1435.
DR   EnsemblBacteria; BAA15068; BAA15068; BAA15068.
DR   GeneID; 945993; -.
DR   KEGG; ecj:JW1431; -.
DR   KEGG; eco:b1435; -.
DR   PATRIC; fig|1411691.4.peg.834; -.
DR   EchoBASE; EB3522; -.
DR   eggNOG; COG0826; Bacteria.
DR   HOGENOM; CLU_011540_5_0_6; -.
DR   InParanoid; P76104; -.
DR   OMA; MKDNNQS; -.
DR   PhylomeDB; P76104; -.
DR   BioCyc; EcoCyc:G6746-MON; -.
DR   BioCyc; MetaCyc:G6746-MON; -.
DR   PRO; PR:P76104; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0000154; P:rRNA modification; IMP:EcoCyc.
DR   InterPro; IPR020988; Pept_U32_collagenase.
DR   InterPro; IPR001539; Peptidase_U32.
DR   Pfam; PF12392; DUF3656; 1.
DR   Pfam; PF01136; Peptidase_U32; 1.
DR   PROSITE; PS01276; PEPTIDASE_U32; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; rRNA processing.
FT   CHAIN           1..653
FT                   /note="23S rRNA 5-hydroxycytidine C2501 synthase"
FT                   /id="PRO_0000028524"
FT   MUTAGEN         161
FT                   /note="E->A: Strong decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:29069499"
FT   MUTAGEN         165
FT                   /note="H->A: No change in activity."
FT                   /evidence="ECO:0000269|PubMed:29069499"
FT   MUTAGEN         169
FT                   /note="C->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:29069499"
FT   MUTAGEN         175
FT                   /note="Q->A: No change in activity."
FT                   /evidence="ECO:0000269|PubMed:29069499"
FT   MUTAGEN         176
FT                   /note="C->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:29069499"
FT   MUTAGEN         580
FT                   /note="C->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:29069499"
FT   MUTAGEN         611
FT                   /note="C->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:29069499"
SQ   SEQUENCE   653 AA;  72702 MW;  5875B4E9C2F4FC82 CRC64;
     MTVSSHRLEL LSPARDAAIA REAILHGADA VYIGGPGFGA RHNASNSLKD IAELVPFAHR
     YGAKIFVTLN TILHDDELEP AQRLITDLYQ TGVDALIVQD MGILELDIPP IELHASTQCD
     IRTVEKAKFL SDVGFTQIVL ARELNLDQIR AIHQATDATI EFFIHGALCV AYSGQCYISH
     AQTGRSANRG DCSQACRLPY TLKDDQGRVV SYEKHLLSMK DNDQTANLGA LIDAGVRSFK
     IEGRYKDMSY VKNITAHYRQ MLDAIIEERG DLARASSGRT EHFFVPSTEK TFHRGSTDYF
     VNARKGDIGA FDSPKFIGLP VGEVVKVAKD HLDVAVTEPL ANGDGLNVLI KREVVGFRAN
     TVEKTGENQY RVWPNEMPAD LHKIRPHHPL NRNLDHNWQQ ALTKTSSERR VAVDIELGGW
     QEQLILTLTS EEGVSITHTL DGQFDEANNA EKAMNNLKDG LAKLGQTLYY ARDVQINLPG
     ALFVPNSLLN QFRREAADML DAARLASYQR GSRKPVADPA PVYPQTHLSF LANVYNQKAR
     EFYHRYGVQL IDAAYEAHEE KGEVPVMITK HCLRFAFNLC PKQAKGNIKS WKATPMQLVN
     GDEVLTLKFD CRPCEMHVIG KIKNHILKMP LPGSVVASVS PDELLKTLPK RKG
 
 
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